Antibodies to HIV-1 gp41 recognize synthetic peptides of human IFN-alpha and IFN-beta

Bai, Y.; Zhao, Y.; Yu, T.; Dierich, M.P.; Chen, Y.H.

International Archives of Allergy and Immunology 121(2): 170-172

2000


ISSN/ISBN: 1018-2438
PMID: 10705228
DOI: 10.1159/000024313
Accession: 010184119

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Abstract
Based on our finding that a common epitope exists between HIV-1 gp41 and human type I interferons (IFN-alpha and IFN-beta), and increased levels of antibodies against human IFN-alpha and IFN-beta were observed in HIV-1-infected individuals, we tried to explain the mechanism of increased levels of antibodies. Mouse antisera recognizing HIV-1 recombinant soluble (rs) gp41 (aa 539-684) interacted with two synthetic peptides sequence-corresponding to the IFN-alpha/beta receptor binding site on human IFN-alpha and IFN-beta, while normal mouse serum (pooled normal sera) did not. The anti-rspg41 antisera after adsorption by IFN-beta sepharose column lost the activity of interaction with both synthetic peptides. In another experiment, rsgp41 could bind to sepharose column conjugated with anti-IFN-beta polyclonal antibodies (IgG). These results indicate that the common epitope on gp41 and type I interferons could induce antibodies recognizing the receptor binding site on IFN-alpha and IFN-beta, suggesting that increased levels of antibodies against IFN-alpha and IFN-beta in HIV-1-infected individuals could be induced by gp41.